C-terminal regions of D-hydantoinases are nonessential for catalysis, but affect the oligomeric structure.
Most microbial D-hydantoinases have been reported to have catalytic properties similar to those of mammalian dihydropyrimidinases. Comparison of the primary structures of microbial D-hydantoinases with mammalian dihydropyrimidinases revealed that the amino acid homology is about 37% and functionally important residues are rigidly conserved at identical positions. Interestingly, however, the C-terminal regions were found to be completely mismatched with each other. In order to investigate the possible role of the C-terminal regions, we deleted the C-terminal regions of the D-hydantoinases from two thermophilic Bacilli and compared the catalytic and structural properties of the mutant enzymes with those of wild-type enzymes. As a result, the C-terminal region was found not to be essential for catalysis, but it does affect the oligomeric structure of the enzyme.
Kim
G J
GJ
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejon, Korea.
Kim
H S
HS
D000581:Amidohydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001407:Bacillus / Q000201:enzymology / Q000235:genetics; D001483:Base Sequence; D001665:Binding Sites; D002384:Catalysis; D017124:Conserved Sequence; D017931:DNA Primers / Q000235:genetics; D001411:Geobacillus stearothermophilus / Q000201:enzymology / Q000235:genetics; D006801:Humans; D011487:Protein Conformation; D051381:Rats; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid
D017931:DNA Primers; D000581:Amidohydrolases; C020047:dihydropyrimidinase